PROTEIN LIPID INTERACTION

这项建议的目的是继续我们的遗传研究。 在几个定义明确的系统中，蛋白质和脂质 互动。这种相互作用对于组装和 生物膜的功能。系统是i) 细菌酶环丙烷脂肪酸合成酶II) 含脂噬菌体PR4和III)的形态发生 苹果酸氧化酶，一种被磷脂激活的酶。 环丙烷脂肪酸合成酶是唯一不连续的酶 已知能与非极性部分发生特异性反应 磷脂双层。我们建议准备大量的 利用重组DNA技术对该酶进行了初步研究 与其磷脂底物的详细相互作用。噬菌体PR4 从细菌膜中获得衣壳类物质，这 过程是研究膜形态发生的一个很好的模型 遗传手段。我们建议结合使用遗传学和 生物化学研究噬菌体脂类的作用机制 都被收购了。苹果酸氧化酶，一项新的项目，是一种酶 被磷脂极大地激活。我们希望分离出突变体 这种酶在激活中有缺陷，通过脂质来确定作用 脂质结合在苹果酸氧化酶功能中的作用。

The aim of this proposal is to continue our study by genetic means of several well-defined systems in which proteins and lipids interact. Such interactions are essential to the assembly and function of biological membranes. The systems are i) the bacterial enzyme cyclopropane fatty acid synthase, ii) morphogenesis of the lipid-containing bacteriophage PR4, and iii) malate oxidase, an enzyme which is activated by phospholipids. Cyclopropane fatty acid synthase is the only discrete enzyme known to specifically react with the nonpolar portion of a phospholipid bilayer. We propose to prepare large quantities of this enzyme by recombinant DNA techniques and to study its detailed interaction with its phospholipid substrate. Phage PR4 acquires its capsid lipid from the bacterial membrane and this process is a good model to study membrane morphogenesis by genetic means. We propose to use a combination of genetics and biochemistry to study the mechanisms whereby the phage lipids are acquired. Malate oxidase, a new project, is an enzyme that is greatly activated by phospholipids. We wish to isolate mutants of this enzyme defective in activation by lipids to determine the role of lipid binding in malate oxidase function.